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http://purl.uniprot.org/citations/7730794http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7730794http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7730794http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/7730794http://www.w3.org/2000/01/rdf-schema#comment"Autographa californica multiple nuclear polyhedrosis virus (AcMNPV) contains a 966 bp ORF that encodes a papain type cysteine proteinase with cathepsin L-like characteristics. Using Western blot analysis of infected cell extracts we showed that v-cath proteinase has 35.5 kDa and 32 kDa precursor forms which are processed to a 27.5 kDa mature form in a manner characteristic of papain and cathepsin L. V-cath proteinase activity was greatest under acidic conditions (pH 5.0) and was reduced in the presence of the cysteine proteinase inhibitors, leupeptin and E64. Urea, a known enhancer of cathepsin L activity, also enhanced v-cath proteinase activity. AcMNPV v-cath proteinase was detected post-mortem in tissues of insects infected with wild-type (wt) virus. Insects infected with a v-cath deletion mutant did not become flaccid after death as is normally observed with wt AcMNPV infections. These findings indicate a link between v-cath activity and degradation of host tissues during virus pathogenesis."xsd:string
http://purl.uniprot.org/citations/7730794http://purl.org/dc/terms/identifier"doi:10.1099/0022-1317-76-5-1091"xsd:string
http://purl.uniprot.org/citations/7730794http://purl.org/dc/terms/identifier"doi:10.1099/0022-1317-76-5-1091"xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/author"Kuzio J."xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/author"Kuzio J."xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/author"Faulkner P."xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/author"Faulkner P."xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/author"Slack J.M."xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/author"Slack J.M."xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/name"J. Gen. Virol."xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/name"J. Gen. Virol."xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/pages"1091-1098"xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/pages"1091-1098"xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/title"Characterization of v-cath, a cathepsin L-like proteinase expressed by the baculovirus Autographa californica multiple nuclear polyhedrosis virus."xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/title"Characterization of v-cath, a cathepsin L-like proteinase expressed by the baculovirus Autographa californica multiple nuclear polyhedrosis virus."xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/volume"76"xsd:string
http://purl.uniprot.org/citations/7730794http://purl.uniprot.org/core/volume"76"xsd:string
http://purl.uniprot.org/citations/7730794http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7730794
http://purl.uniprot.org/citations/7730794http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7730794
http://purl.uniprot.org/citations/7730794http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7730794